| 4-hydroxy-4-methyl-2-oxoglutarate aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.3.17 | ||||||||
| CAS no. | 37290-65-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme 4-hydroxy-4-methyl-2-oxoglutarate aldolase ( EC 4.1.3.17) catalyzes the chemical reaction
- 4-hydroxy-4-methyl-2-oxoglutarate 2 pyruvate
This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase (pyruvate-forming). Other names in common use include pyruvate aldolase, gamma-methyl-gamma-hydroxy-alpha-ketoglutaric aldolase, 4-hydroxy-4-methyl-2-ketoglutarate aldolase, and 4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase. This enzyme participates in benzoate degradation via hydroxylation and c5-branched dibasic acid metabolism.
- Maruyama K (February 1983). "Purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase". J. Biochem. 93 (2). Tokyo: 557–65. PMID 6841353.
- Sharma ML, Kaul SM, Shukla OP (1984). "Metabolism of 2-hydroxypyridine by Bacillus brevis (INA)". Biol. Membr. 9: 43–52.
- Tack BF, Chapman PJ, Dagley S (1972). "Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase". J. Biol. Chem. 247 (20): 6444–9. PMID 5076765.
- Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 7, Academic Press, New York, 1972, p. 281-302.
| 4-hydroxy-4-methyl-2-oxoglutarate aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.3.17 | ||||||||
| CAS no. | 37290-65-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The enzyme 4-hydroxy-4-methyl-2-oxoglutarate aldolase ( EC 4.1.3.17) catalyzes the chemical reaction
- 4-hydroxy-4-methyl-2-oxoglutarate 2 pyruvate
This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase (pyruvate-forming). Other names in common use include pyruvate aldolase, gamma-methyl-gamma-hydroxy-alpha-ketoglutaric aldolase, 4-hydroxy-4-methyl-2-ketoglutarate aldolase, and 4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase. This enzyme participates in benzoate degradation via hydroxylation and c5-branched dibasic acid metabolism.
- Maruyama K (February 1983). "Purification and properties of 2-pyrone-4,6-dicarboxylate hydrolase". J. Biochem. 93 (2). Tokyo: 557–65. PMID 6841353.
- Sharma ML, Kaul SM, Shukla OP (1984). "Metabolism of 2-hydroxypyridine by Bacillus brevis (INA)". Biol. Membr. 9: 43–52.
- Tack BF, Chapman PJ, Dagley S (1972). "Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase". J. Biol. Chem. 247 (20): 6444–9. PMID 5076765.
- Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 7, Academic Press, New York, 1972, p. 281-302.